[beta-1,3-1,4-glucanase in spore-forming microorganisms. IV. Properties of some Bacillus-beta-glucan-hydrolases (author's transl)].
The beta-glucan-hydrolases produced by seven Bacillus species have been characterized with regard to some physicochemical properties. Ca-ions stabilize all tested glucanases. Optimum pH and optimum temperature were found to be different for the investigated enzymes. In the work presented here is given further characteristics of Bacillus-beta-glucan-hydrolases as pH-stability and temperature stability, sensibility on glucono-1,5-lactone, as well known inhibitor of carbohydrases, and electrophoretic mobility on cellulose acetate-sheets.
D001407:Bacillus / Q000201:enzymology*; D001412:Bacillus subtilis / Q000201:enzymology*; D002118:Calcium / Q000494:pharmacology; D004588:Electrophoresis, Cellulose Acetate; D005942:Gluconates / Q000494:pharmacology; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007783:Lactones / Q000494:pharmacology; D013696:Temperature
D005942:Gluconates; D007783:Lactones; D006026:Glycoside Hydrolases; C028020:licheninase; D002118:Calcium; C010730:beta-glucono-1,5-lactone
beta-1,3-1,4-Glucanase in sporenbildenden Mikroorganismen. IV. Eigenschaften einiger Bacillus-beta-Glucan-HER.